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Nick Hud Appointed as Regents Professor

The title represents the highest academic recognition bestowed by the University System of Georgia, and demonstrate distinction and achievement in teaching and scholarly research.

Working with Pharmaceutical Industry Professionals Before Graduation

GlaxoSmithKline co-op program gives Ph.D. chemistry student Cynthia Martin real-life training in drug discovery.

Seminars & Events

Prof. Joshua Pierce - North Carolina State University
Organic Division Seminar - Tuesday, September 27, 2016 - 4:00pm - MoSE 3201A
Michael Burkart - UC San Diego
Colloquium - Thursday, October 6, 2016 - 4:00pm - MoSe G011
Andrei Yudin - University of Toronto
Colloquium - Thursday, October 13, 2016 - 4:00pm - MoSe G011
Meeting - Tuesday, October 18, 2016 - 11:00am - MoSE 3201A

Featured Research

Article Title
Research Authors
Venkatakrishnan, Balasubramanian; Katen, Sarah P.; Francis, Samson; Chirapu, Srinivas; Finn, M. G.; Zlotnick, Adam.
Citation
Journal of Virology (2016), Vol. 90(8), 3994-4004
Miscellaneous Details
Macromolecular Crystallography Facility at Indiana University, Bloomington. BioCARS staff at beamline 14BM-C at the Advanced Photon Source, Argonne National Laboratory, for assistance with data collection

Though the hepatitis B virus (HBV) core protein is an important participant in many aspects of the viral life cycle, its best-characterized activity is self-assembly into 240-monomer capsids. Small molecules that target core protein (core protein allosteric modulators [CpAMs]) represent a promising antiviral strategy. To better understand the structural basis of the CpAM mechanism, we determined the crystal structure of the HBV capsid in complex with HAP18. HAP18 accelerates assembly, increases protein-protein association more than 100-fold, and induces assembly of nonicosahedral macrostructures. In a preformed capsid, HAP18 is found at quasiequivalent subunit-subunit interfaces. In a detailed comparison to the two other extant CpAM structures, we find that the HAP18-capsid structure presents a paradox. Whereas the two other structures expanded the capsid diameter by up to 10 angstrom, HAP18 caused only minor changes in quaternary structure and actually decreased the capsid diameter by similar to 3 angstrom. These results indicate that CpAMs do not have a single allosteric effect on capsid structure. We suggest that HBV capsids present an ensemble of states that can be trapped by CpAMs, indicating a more complex basis for antiviral drug design.

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